ArticleThe Journal of biological chemistry2013
Basic properties of rotary dynamics of the molecular motor Enterococcus hirae V1-ATPase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 59 citations in OpenAlex.
- A minimal chemo-mechanical Markov model for rotary catalysis of FNature communications · 2026Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- ATP synthesis of Enterococcus hirae V-ATPase driven by sodium motive force.The Journal of biological chemistry · 2025Article
- NaNature structural & molecular biology · 2025Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Design of allosteric sites into rotary motor VNature chemistry · 2023Article
- Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover.Communications biology · 2023Article
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Revealing a Hidden Intermediate of Rotatory Catalysis with X-ray Crystallography and Molecular Simulations.ACS central science · 2022Article
- Scattering-based Light Microscopy: From Metal Nanoparticles to Single Proteins.Chemical reviews · 2021Review
- The catalytic dwell in ATPases is not crucial for movement against applied torque.Nature chemistry · 2020Article
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking.Scientific reports · 2020Article
- Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme ofThe Journal of biological chemistry · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Metastable asymmetrical structure of a shaftless VScience advances · 2019Article
- Rotational Mechanism Model of the Bacterial VFrontiers in physiology · 2019Review
- Single-Nanoparticle Tracking with Angstrom Localization Precision and Microsecond Time Resolution.Biophysical journal · 2018Article
- Structure and dynamics of rotary VCellular and molecular life sciences : CMLS · 2018Review
- VGLUT1 functions as a glutamate/proton exchanger with chloride channel activity in hippocampal glutamatergic synapses.Nature communications · 2017Article
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
V-ATPases are rotary molecular motors that generally function as proton pumps. We recently solved the crystal structures of the V1 moiety of Enterococcus hirae V-ATPase (EhV1) and proposed a model for its rotation mechanism. Here, we characterized the rotary dynamics of EhV1 using single-molecule analysis employing a load-free probe. EhV1 rotated in a counterclockwise direction, exhibiting two distinct rotational states, namely clear and unclear, suggesting unstable interactions between the rotor and stator. The clear state was analyzed in detail to obtain kinetic parameters. The rotation rates obeyed Michaelis-Menten kinetics with a maximal rotation rate (Vmax) of 107 revolutions/s and a Michaelis constant (Km) of 154 μM at 26 °C. At all ATP concentrations tested, EhV1 showed only three pauses separated by 120°/turn, and no substeps were resolved, as was the case with Thermus thermophilus V1-ATPase (TtV1). At 10 μM ATP (<<Km), the distribution of the durations of the ATP-waiting pause fit well with a single-exponential decay function. The second-order binding rate constant for ATP was 2.3 × 10(6) M(-1) s(-1). At 40 mM ATP (>>Km), the distribution of the durations of the catalytic pause was reproduced by a consecutive reaction with two time constants of 2.6 and 0.5 ms. These kinetic parameters were similar to those of TtV1. Our results identify the common properties of rotary catalysis of V1-ATPases that are distinct from those of F1-ATPases and will further our understanding of the general mechanisms of rotary molecular motors.
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